Publications
Title | Abstract | Year Filter | PMID(sorted descending) Filter |
---|
unexpected no-dependent dna binding by the cooa homolog from carboxydothermus hydrogenoformans. | cooa, the co-sensing heme protein from rhodospirillum rubrum, regulates the expression of genes that encode a co-oxidation system, allowing r. rubrum to use co as a sole energy source. to better understand the gas-sensing regulation mechanism used by r. rubrum cooa and its homologs in other organisms, we characterized spectroscopically and functionally the fe(ii), fe(ii)-no, and fe(ii)-co forms of cooa from carboxydothermus hydrogenoformans. surprisingly, and unlike r. rubrum cooa, c. hydrogenof ... | 2006 | 16410360 |
comparative study of spectral flexibilities of bacterial light-harvesting complexes: structural implications. | this work presents a comparative study of the frequencies of spectral jumping of individual light-harvesting complexes of six different types: lh2 of rhodopseudomonas acidophila, rhodobacter sphaeroides, and rhodospirillum molischianum; lh1 of rhodobacter sphaeroides; and two "domain swap mutants" of lh2 of rhodobacter sphaeroides: paclh1 and paclh2mol, in which the alpha-polypeptide c-terminus is exchanged with the corresponding sequence from lh1 of rhodobacter sphaeroides or lh2 of rhodospiril ... | 2006 | 16399835 |
spectral trends in the fluorescence of single bacterial light-harvesting complexes: experiments and modified redfield simulations. | in this work we present and discuss the single-molecule fluorescence spectra of a variety of species of light-harvesting complexes: lh2 of rhodopseudomonas acidophila, rhodobacter sphaeroides, and rhodospirillum molischianum and lh1 of rhodobacter sphaeroides. the emission spectrum of these complexes varies as a function of time as was described in earlier work. for each type of complex, we observe a pronounced and well-reproducible characteristic relationship between the fluorescence spectral p ... | 2006 | 16399834 |
increased nitrogenase-dependent h(2) photoproduction by hup mutants of rhodospirillum rubrum. | transposon tn5 mutagenesis was used to isolate mutants of rhodospirillum rubrum which lack uptake hydrogenase (hup) activity. three tn5 insertions mapped at different positions within the same 13-kb ecori fragment (fragment e1). hybridization experiments revealed homology to the structural hydrogenase genes hupslm from rhodobacter capsulatus and hupsl from bradyrhizobium japonicum in a 3.8-kb ecori-clai subfragment of fragment e1. it is suggested that this region contains at least some of the st ... | 1994 | 16349271 |
optimization of the sistrom culture medium for large-scale batch cultivation of rhodospirillum rubrum under semiaerobic conditions with maximal yield of photosynthetic membranes. | the defined medium a of w. r. sistrom (w. r. sistrom, j. gen. microbiol. 22:77-85, 1960) has been modified to allow the growth of rhodospirillum rubrum in large-scale batch cultures under dark, semiaerobic conditions. the simultaneous use of two substrates, nh(4)-succinate (46 mm) and fructose (0.3%), which are utilized in aerobic and fermentative metabolism, respectively, leads to very high cell densities with a maximal yield of photosynthetic membranes. | 1994 | 16349265 |
modification of the fe protein of nitrogenase in natural populations of trichodesmium thiebautii. | the fe protein of nitrogenase in the marine nonheterocystous cyanobacterium trichodesmium thiebautii is interconverted between two forms, which is reminiscent of the adp-ribosylation described in the purple bacterium rhodospirillum rubrum. in natural populations of t. thiebautii during the day, when nitrogenase activity (na) is present and while photosynthetic rates are high, a low-molecular-mass form of the fe protein is present. in the late afternoon, the low-molecular-mass form is partially c ... | 1993 | 16348883 |
populations of anaerobic phototrophic bacteria in a spartina alterniflora salt marsh. | habitat-simulating media were used with the hungate anaerobic roll tube technique to enumerate culturable anaerobic photosynthetic bacteria in sediment, tidal waters, and spartina alterniflora plant samples collected from the salt marsh at sapelo island, ga. no phototrophs were detected in samples of creekside (low marsh) sediment or in tidal waters in creekside regions. in the high marsh region, 90% of anaerobic phototrophic bacteria occurred in the top 5 mm of sediment and none were detected b ... | 1988 | 16347646 |
hydrogen production by the photosynthetic bacterium rhodospirillum rubrum. | continuous photosynthetic production of hydrogen by rhodospirillum rubrum in batch cultures was observed up to 80 days with the hydrogen donor, pure lactate or lactic acid-containing wastes, supplied periodically. hydrogen was produced at an average rate of 6 ml/h per g (dry weight) of cells with whey as a hydrogen donor. in continuous cultures with glutamate as a growth-limiting nitrogen source and lactate as a hydrogen donor, hydrogen was evolved at a rate of 20 ml/h per g (dry weight). the co ... | 1979 | 16345375 |
architecture of the native photosynthetic apparatus of phaeospirillum molischianum. | the ubiquity and importance of photosynthetic organisms in nature has made the molecular mechanisms of photosynthesis a widely studied subject at both structural and functional levels. a current challenge is to understand the supramolecular assembly of the proteins involved in photosynthesis in native membranes. we have used atomic force microscopy to study the architecture of the photosynthetic apparatus and analyze the structure of single molecules in chromatophores of phaeospirillum molischia ... | 2005 | 16330228 |
new insights into the mechanism of nickel insertion into carbon monoxide dehydrogenase: analysis of rhodospirillum rubrum carbon monoxide dehydrogenase variants with substituted ligands to the [fe3s4] portion of the active-site c-cluster. | carbon monoxide dehydrogenase (codh) from rhodospirillum rubrum catalyzes the oxidation of co to co2. a unique [nife4s4] cluster, known as the c-cluster, constitutes the active site of the enzyme. when grown in ni-deficient medium r. rubrum accumulates a ni-deficient apo form of codh that is readily activated by ni. it has been previously shown that activation of apo-codh by ni is a two-step process involving the rapid formation of an inactive apo-codh*ni complex prior to conversion to the activ ... | 2005 | 16283394 |
isotopic labeling of proteins by utilizing photosynthetic bacteria. | 2005 | 16259936 | |
re-identification of the n-terminal amino acid residue and its modification of +/-bbeta-polypeptide of light-harvesting complex i from rhodospirillum rubrum. | 2001 | 16252177 | |
nitrogen fixation by photosynthetic bacteria. | in 1949, howard gest and martin kamen published two brief papers in science that changed our perceptions about the metabolic capabilities of photosynthetic bacteria. their discovery of photoproduction of hydrogen and the ability of rhodospirillum rubrum to fix nitrogen led to a greater understanding of both processes. | 2002 | 16245111 |
purification and characterization of the polypeptides of core light-harvesting complexes from purple sulfur bacteria. | although the polypeptides of core light-harvesting complexes (lh1) from many purple nonsulfur bacteria have been well characterized, little information is available on the polypeptides of lh1 from purple sulfur photosynthetic organisms. we present here the results of isolation and characterization of lh1 polypeptides from two purple sulfur bacteria, thermochromatium (tch.) tepidum and allochromatium (ach.) vinosum. native lh1 complexes were extracted and purified in a reaction center (rc)-associ ... | 2003 | 16245044 |
reversible membrane association of dinitrogenase reductase activating glycohydrolase in the regulation of nitrogenase activity in rhodospirillum rubrum; dependence on glnj and amtb1. | in the photosynthetic bacterium rhodospirillum rubrum nitrogenase activity is regulated by reversible adp-ribosylation of dinitrogenase reductase in response to external so called "switch-off" effectors. activation of the modified, inactive form is catalyzed by dinitrogenase reductase activating glycohydrolase (drag) which removes the adp-ribose moiety. this study addresses the signal transduction between external effectors and drag. r. rubrum, wild-type and p(ii) mutant strains, were studied wi ... | 2005 | 16243452 |
investigations of intermediates appearing in the reassociation of the light-harvesting 1 complex of rhodospirillum rubrum. | we investigated the temperature-mediated reassociation of the b820 subunit of rs. rubrum to form a light-harvesting 1 complex (lh 1). by combining several spectroscopic techniques with global spectral data analysis fitting, we present evidence for the occurence of two spectral intermediates that appear during the reassociation process. at high temperatures, halfway the reassociation reaction, a prominent intermediate appears that has an absorption maximum around 850 nm, a fluorescence maximum ar ... | 2003 | 16228604 |
interaction of bacteriochlorophyll with the lh1 and pufx polypeptides of photosynthetic bacteria: use of chemically synthesized analogs and covalently attached fluorescent probes. | the protein components of the reaction center (rc) and core light-harvesting (lh 1) complexes of photosynthetic bacteria have evolved to specifically, but non-covalently, bind bacteriochlorophyll (bchl). the contribution to binding of specific structural elements in the protein and bchl may be determined for the lh 1 complex because its subunit can be studied by reconstitution under equilibrium conditions. important to the determination and utilization of such information is the characterization ... | 2003 | 16228601 |
cloning, sequencing and analysis of the pucc genes from rubrivivax gelatinosus strain 151 and rhodopseudomonas acidophila strain 10050. | the pucc genes of rubrivivax gelatinosus strain 151 and rhodopseudomonas acidophila strain 10050 have been identified, cloned and sequenced. in rubrivivax gelatinosus the arrangement of the pucc gene with regard to the pucba genes was shown to differ from that found in other species of photosynthetic bacteria. the rhodopseudomonas acidophila pucc was found downstream of four new pucba gene pairs, bringing the sequenced pucba pairs to a total of eight in this strain. the predicted pucc protein se ... | 2000 | 16228472 |
efficient light harvesting through carotenoids. | we review the factors that control the efficiency of carotenoid-chlorophyll excitation transfer in photosynthetic light harvesting. for this we summarize first the recently developed theory that describes electronic couplings between carotenoids and chlorophylls and we outline in particular the influence of length of conjugated system and of symmetry breaking on the couplings. we focus hereby on the structurally solved lycopene-bchl system of lh 2 from rhodospirillum molischianum and the peridin ... | 2000 | 16228415 |
nad-, nmn-, and nadp-dependent modification of dinitrogenase reductases from rhodospirillum rubrum and azotobacter vinelandii. | nitrogenase activity in the photosynthetic bacterium rhodospirillum rubrum is reversibly regulated by adp-ribosylation of a specific arginine residue of dinitrogenase reductase based on the cellular nitrogen or energy status. in this paper, we have investigated the ability of nicotinamide adenine dinucleotide, nad (the physiological adp-ribose donor), and its analogs to support covalent modification of dinitrogenase reductase in vitro. r. rubrum dinitrogenase reductase can be modified by drat in ... | 2005 | 16225869 |
the pufx protein of rhodobacter capsulatus affects the properties of bacteriochlorophyll a and carotenoid pigments of light-harvesting complex 1. | a pufx gene deletion in the purple bacterium rhodobacter capsulatus causes a severe photosynthetic defect and increases core light-harvesting complex (lh1) protein and bacteriochlorophyll a (bchl) levels. it was suggested that pufx interrupts the lh1 alpha/beta ring around the reaction centre, allowing quinone/quinol exchange. however, naturally pufx(-) purple bacteria grow photosynthetically with an uninterrupted lh1. we discovered that substitutions of the rhodobacter-specific lh1 alpha seryl- ... | 2005 | 16212932 |
heme-thiolate proteins. | cytochrome p450 was the first hemoprotein found to have a thiolate anion as the axial ligand of the heme. several other heme-thiolate proteins, including nitric oxide synthase, were later found in animals, plants, and microorganisms. both cytochrome p450 and nitric oxide synthase, two major members of the heme-thiolate protein family, catalyze monooxygenase reactions, but the physiological functions of other heme-thiolate proteins are apparently highly diverse. chloroperoxidase of a mold, caldar ... | 2005 | 16198303 |
defluvicoccus vanus gen. nov., sp. nov., a novel gram-negative coccus/coccobacillus in the 'alphaproteobacteria' from activated sludge. | a novel gram-negative coccus/coccobacillus, strain ben 114(t), growing in tetrads, clusters or aggregates, was isolated from activated sludge by micromanipulation. 16s rrna gene sequence analysis revealed that it belonged to the 'alphaproteobacteria', with no close relatives among cultured bacterial isolates. on the basis of phylogenetic data, this organism is considered to belong to a new genus, defluvicoccus, represented by the species defluvicoccus vanus sp. nov., a name chosen because of the ... | 2005 | 16166717 |
whole-genome shotgun optical mapping of rhodospirillum rubrum. | rhodospirillum rubrum is a phototrophic purple nonsulfur bacterium known for its unique and well-studied nitrogen fixation and carbon monoxide oxidation systems and as a source of hydrogen and biodegradable plastic production. to better understand this organism and to facilitate assembly of its sequence, three whole-genome restriction endonuclease maps (xbai, nhei, and hindiii) of r. rubrum strain atcc 11170 were created by optical mapping. optical mapping is a system for creating whole-genome o ... | 2005 | 16151144 |
[the mechanism of acetate assimilation in purple nonsulfur bacteria lacking the glyoxylate pathway: enzymes of the citramalate cycle in rhodobacter sphaeroides]. | the mechanism of acetate assimilation by the purple nonsulfur bacterium rhodobacter sphaeroides, which lacks the glyoxylate shortcut, has been studied. in a previous work, proceeding from data on acetate assimilation by rba. sphaeroides cell suspensions, a suggestion was made regarding the operation, in this bacterium, of the citramalate cycle. this cycle was earlier found in rhodospirillum rubrum in the form of an anaplerotic reaction sequence that operates during growth on acetate instead of t ... | 2005 | 16119844 |
multivariate analysis of single-molecule spectra: surpassing spectral diffusion. | the full exploitation of single-molecule spectroscopy in disordered systems is often hampered by spectral diffusion processes of the optical transitions due to structural fluctuations in the local environment of the probe molecule which leads to temporal averaging of the signal. multivariate statistical pattern recognition techniques, originally developed for single-molecule cryoelectron microscopy, allow us to retrieve detailed information from optical single-molecule spectra. as an example, we ... | 2005 | 16090183 |
x-ray structure of domain i of the proton-pumping membrane protein transhydrogenase from escherichia coli. | the dimeric integral membrane protein nicotinamide nucleotide transhydrogenase is required for cellular regeneration of nadph in mitochondria and prokaryotes, for detoxification and biosynthesis purposes. under physiological conditions, transhydrogenase couples the reversible reduction of nadp+ by nadh to an inward proton translocation across the membrane. here, we present crystal structures of the nad(h)-binding domain i of transhydrogenase from escherichia coli, in the absence as well as in th ... | 2005 | 16083909 |
detecting proton flux across chromatophores driven by f0f1-atpase using n-(fluorescein-5-thiocarbamoyl)-1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine, triethylammonium salt. | n-(fluorescein-5-thiocarbamoyl)-1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine, triethylammonium salt (f-dhpe) is a lipid fluorescence dye sensitive to ph changes and is used in this study for detecting proton flux through f0f1-atpase within chromatophores driven by atp hydrolysis. f-dhpe is easily labeled to the outer surface of chromatophores. in the range of ph 7.0 to 9.0, fluorescence intensity is sensitive to ph changes. the sensitivity is especially great in the range of ph 8.2 to 9.0 ... | 2005 | 16043113 |
chromatic adaptation of photosynthetic membranes. | many biological membranes adapt in response to environmental conditions. we investigated how the composition and architecture of photosynthetic membranes of a bacterium change in response to light, using atomic force microscopy. despite large modifications in the membrane composition, the local environment of core complexes remained unaltered, whereas specialized paracrystalline light-harvesting antenna domains grew under low-light conditions. thus, the protein mixture in the membrane shows eute ... | 2005 | 16020739 |
tributyl phosphate degradation by rhodopseudomonas palustris and other photosynthetic bacteria. | tributyl phosphate (tbp) is widely used in nuclear fuel processing and other waste generating chemical industries. although tbp is bacteriostatic, some microbes are resistant to it and may degrade it. under dark aerobiosis, purple non-sulfur photosynthetic bacteria degraded up to 0.6 mm tbp, initially present at 2 mm, within 3 weeks and under photosynthetic conditions, rhodopseudomonas palustris degraded 1.6 mm tbp within 3 weeks. the curing of the rhodopseudomonas palustris endogenous plasmid d ... | 2005 | 15973490 |
watching the components of photosynthetic bacterial membranes and their in situ organisation by atomic force microscopy. | the atomic force microscope has developed into a powerful tool in structural biology allowing information to be acquired at submolecular resolution on the protruding structures of membrane proteins. it is now a complementary technique to x-ray crystallography and electron microscopy for structure determination of individual membrane proteins after extraction, purification and reconstitution into lipid bilayers. moving on from the structures of individual components of biological membranes, atomi ... | 2005 | 15919049 |
involvement of a che-like signal transduction cascade in regulating cyst cell development in rhodospirillum centenum. | homologues of the e. coli chemotaxis (che) signal transduction pathway are present in nearly all motile bacteria. although e. coli contains only one che cascade, many other bacteria are known to possess multiple sets of che genes. the role of multiple che-like gene clusters could potentially code for parallel che-like signal transduction pathways that have distinctly different input and output functions. in this study, we describe a che-like gene cluster in rhodospirillum centenum that controls ... | 2005 | 15916598 |
zinc ions selectively inhibit steps associated with binding and release of nadp(h) during turnover of proton-translocating transhydrogenase. | transhydrogenase couples the redox reaction between nad(h) and nadp(h) to proton translocation across a membrane. in membrane vesicles from escherichia coli and rhodospirillum rubrum, the transhydrogenase reaction (measured in the direction driving inward proton translocation) was inhibited by zn(2+) and cd(2+). however, depending on ph, the metal ions either had no effect on, or stimulated, "cyclic" transhydrogenation. they must, therefore, interfere specifically with steps involving binding/re ... | 2005 | 15878164 |
titration of e. coli transhydrogenase domain iii with bound nadp+ or nadph studied by nmr reveals no ph-dependent conformational change in the physiological ph range. | a ph-titration 2d nmr study of escherichia coli transhydrogenase domain iii with bound nadp(+) or nadph has been carried out, in which the ph was varied between 5.4 and 12. in this analysis, individual amide protons served as reporter groups. the apparent pk(a) values of the amide protons, determined from the ph-dependent chemical shift changes, were attributed to actual pk(a) values for several titrating residues in the protein. the essential asp392 is shown to be protonated at neutral ph in bo ... | 2004 | 15863102 |
electron transport to nitrogenase in rhodospirillum rubrum: identification of a new fdxn gene encoding the primary electron donor to nitrogenase. | in our efforts to determine the components participating in the electron transport to nitrogenase in rhodospirillum rubrum, we have identified a gene encoding a new ferredoxin. we have generated mutants in both the new ferredoxin and ferredoxin i and demonstrate that the new ferredoxin, fdn and not the previously identified fdi is the main donor of electrons to nitrogenase. | 2005 | 15837392 |
dual roles of an e-helix residue, glu167, in the transcriptional activator function of cooa. | cooa is a transcriptional activator that mediates co-dependent expression of the genes responsible for co oxidation in rhodospirillum rubrum. in this study, we suggest in vitro and in vivo models explaining an unusual requirement of cooa for millimolar levels of divalent cations for high-affinity dna binding. several lines of evidence indicate that an e-helix residue, glu167, plays a central role in this requirement by inhibiting sequence-specific dna binding via charge repulsion in the absence ... | 2005 | 15805503 |
trapping of an assembly intermediate of photosynthetic lh1 antenna beyond b820 subunit. significance for the assembly of photosynthetic lh1 antenna. | most photosynthetic lh1 antennae undergo dissociation into b820 subunits, suggesting their universal character as structural modules. however, dissociation into subunits seems to occur reversibly only in the absence of carotenoids and the subunits were never found to bind carotenoids. the interactions of carotenoids with b820 have been studied in a newly developed reconstitution assay of the lh1 antenna from rhodospirillum rubrum (fiedor, l., akahane, j., and koyama, y. (2004) biochemistry 43, 1 ... | 2005 | 15788392 |
near-ir absorption and fluorescence spectra and afm observation of the light-harvesting 1 complex on a mica substrate refolded from the subunit light-harvesting 1 complexes of photosynthetic bacteria rhodospirillum rubrum. | the subunit light-harvesting 1 (lh 1) complexes isolated from photosynthetic bacteria rhodospirillum rubrum using n-octyl-beta-glucoside were reassociated and adsorbed on a mica substrate using spin-coat methods with the aim of using this lh complex in a nanodevice. the near-ir absorption and fluorescence spectra of the lh 1 complexes indicated that the lh 1 complex on the mica was stable, and efficient energy transfer from a carotenoid to a bacteriochlorophyll a was observed. atomic force micro ... | 2005 | 15779986 |
the presumptive magnetosome protein mms16 is a poly(3-hydroxybutyrate) granule-bound protein (phasin) in magnetospirillum gryphiswaldense. | the mms16 protein has been previously found to be associated with isolated magnetosomes from two magnetospirillum strains. a function of this protein as a magnetosome-specific gtpase involved in the formation of intracellular magnetosome membrane vesicles was suggested. here we present a study of the mms16 protein from magnetospirillum gryphiswaldense to clarify its function. insertion-duplication mutagenesis of the mms16 gene did not affect the formation of magnetosome particles but resulted in ... | 2005 | 15774885 |
fluorescence microscopical investigation of poly(3-hydroxybutyrate) granule formation in bacteria. | the early stages of poly(3-hydroxybutyrate) (phb) accumulation were analyzed in vivo by fluorescence microscopy in rhodospirillum rubrum, ralstonia eutropha, and in recombinant escherichia coli harboring the phb biosynthesis genes phacab of r. eutropha. phb granules were stained with nile red and by expression of a phasin-enhanced yellow fluorescent protein fusion protein. distribution of phb granules at the early stages of phb accumulation frequently occurred near the cell poles and near the ce ... | 2005 | 15762619 |
solution structures of the core light-harvesting alpha and beta polypeptides from rhodospirillum rubrum: implications for the pigment-protein and protein-protein interactions. | we have determined the solution structures of the core light-harvesting (lh1) alpha and beta-polypeptides from wild-type purple photosynthetic bacterium rhodospirillum rubrum using multidimensional nmr spectroscopy. the two polypeptides form stable alpha helices in organic solution. the structure of alpha-polypeptide consists of a long helix of 32 amino acid residues over the central transmembrane domain and a short helical segment at the n terminus that is followed by a three-residue loop. pigm ... | 2005 | 15740753 |
a che-like signal transduction cascade involved in controlling flagella biosynthesis in rhodospirillum centenum. | rhodospirillum centenum is a photosynthetic bacterium capable of undergoing swim cell to swarm cell differentiation that allows this species to be motile on both liquid and solid media. previous experiments have demonstrated that the che1 operon is required for the control of chemotactic and phototactic behaviour of both swim and swarm cells. in this report, we analyse the function of a second che-like gene cluster in r. centenum, the che2 gene cluster. in-frame deletion mutants of chew2, cheb2, ... | 2005 | 15720548 |
no evidence for a forced-unfolding mechanism during atp/groes binding to substrate-bound groel: no observable protection of metastable rubisco intermediate or groel-bound rubisco from tritium exchange. | in tritium-hydrogen exchange experiments, the large groel substrate rubisco was unfolded and exchanged in urea/acid/tritiated water, then diluted into either protic buffer or protic buffer containing groel. the respective rubisco metastable folding intermediate or rubisco-groel binary complex was then separated from residual tritium after varying times of exchange by centrifugation through p-10 or g-25 resin. no significant tritium was recovered in either case, in contrast to an earlier report. ... | 2005 | 15710410 |
l-malyl-coenzyme a/beta-methylmalyl-coenzyme a lyase is involved in acetate assimilation of the isocitrate lyase-negative bacterium rhodobacter capsulatus. | cell extracts of rhodobacter capsulatus grown on acetate contained an apparent malate synthase activity but lacked isocitrate lyase activity. therefore, r. capsulatus cannot use the glyoxylate cycle for acetate assimilation, and a different pathway must exist. it is shown that the apparent malate synthase activity is due to the combination of a malyl-coenzyme a (coa) lyase and a malyl-coa-hydrolyzing enzyme. malyl-coa lyase activity was 20-fold up-regulated in acetate-grown cells versus glucose- ... | 2005 | 15687206 |
the puhb protein of rhodobacter capsulatus functions in photosynthetic reaction center assembly with a secondary effect on light-harvesting complex 1. | the core of the photosynthetic apparatus of purple photosynthetic bacteria such as rhodobacter capsulatus consists of a reaction center (rc) intimately associated with light-harvesting complex 1 (lh1) and the pufx polypeptide. the abundance of the rc and lh1 components was previously shown to depend on the product of the puhb gene (formerly known as orf214). we report here that disruption of puhb diminishes rc assembly, with an indirect effect on lh1 assembly, and reduces the amount of pufx. und ... | 2005 | 15687197 |
glnd is essential for nifa activation, ntrb/ntrc-regulated gene expression, and posttranslational regulation of nitrogenase activity in the photosynthetic, nitrogen-fixing bacterium rhodospirillum rubrum. | glnd is a bifunctional uridylyltransferase/uridylyl-removing enzyme and is thought to be the primary sensor of nitrogen status in the cell. it plays an important role in nitrogen assimilation and metabolism by reversibly regulating the modification of p(ii) proteins, which in turn regulate a variety of other proteins. we report here the characterization of glnd mutants from the photosynthetic, nitrogen-fixing bacterium rhodospirillum rubrum and the analysis of the roles of glnd in the regulation ... | 2005 | 15687189 |
conformational diversity in nad(h) and interacting transhydrogenase nicotinamide nucleotide binding domains. | transhydrogenase (th) couples direct and stereospecific hydride transfer between nad(h) and nadp(h), bound within soluble domains i and iii, respectively, to proton translocation across membrane bound domain ii. the cocrystal structure of rhodospirillum rubrum th domains i and iii has been determined in the presence of limiting nadh, under conditions in which the subunits reach equilibrium during crystallization. the crystals contain three heterotrimeric complexes, di(2)diii, in the asymmetric u ... | 2004 | 15670609 |
combined afm and confocal fluorescence microscope for applications in bio-nanotechnology. | we present a custom-designed atomic force fluorescence microscope (affm), which can perform simultaneous optical and topographic measurements with single molecule sensitivity throughout the whole visible to near-infrared spectral region. integration of atomic force microscopy (afm) and confocal fluorescence microscopy combines the high-resolution topographical imaging of afm with the reliable (bio)-chemical identification capability of optical methods. the affm is equipped with a spectrograph en ... | 2005 | 15655068 |
carotenoid-induced cooperative formation of bacterial photosynthetic lh1 complex. | a simple reconstitution technique has been developed and then applied to prepare a series of light-harvesting antenna 1 (lh1) complexes with a programmed carotenoid composition, not available from native photosynthetic membranes. the complexes were reconstituted with different c(40) carotenoids, having two structural parameters variable: the functional side groups and the number of conjugated c-c double bonds, systematically increasing from 9 to 13. the complexes, differing only in the type of c ... | 2004 | 15610043 |
cooa, a paradigm for gas sensing regulatory proteins. | the heme-containing transcriptional factor cooa regulates the expression of genes involved in the oxidation of carbon monoxide (co) in the bacterium rhodospirillum rubrum. cooa is both a redox sensor and a specific co sensor, a combination of properties that is unique among heme proteins. extensive biochemical and genetic analyses, interpreted in the context of a crystal structure of one form of the protein, have allowed the creation of hypotheses concerning the mechanism of cooa activation by c ... | 2005 | 15598507 |
spectroscopic and redox properties of a cooa homologue from carboxydothermus hydrogenoformans. | cooa is a co-sensing transcriptional activator that contains a b-type heme as the active site for sensing its physiological effector, co. in this study, the spectroscopic and redox properties of a new cooa homologue from carboxydothermus hydrogenoformans (ch-cooa) were studied. spectroscopic and mutagenesis studies revealed that his-82 and the n-terminal alpha-amino group were the axial ligands of the fe(iii) and fe(ii) hemes in ch-cooa and that the n-terminal alpha-amino group was replaced by c ... | 2005 | 15537640 |
investigation of the role of the n-terminal proline, the distal heme ligand in the co sensor cooa. | a unique feature of cooa, a heme-containing transcription factor, is that the n-terminal proline is the distal heme ligand in the ferrous state, and this ligand is displaced upon co binding. to investigate the importance of pro(2) in co-dependent dna binding, several cooa variants that alter n-terminal ligation were characterized. electronic absorption, electron paramagnetic resonance, and magnetic circular dichroism spectra of these variants provide the most definitive evidence that pro(2) is t ... | 2004 | 15518565 |
fluorescence spectroscopy of conformational changes of single lh2 complexes. | we have investigated the energy landscape of the bacterial photosynthetic peripheral light-harvesting complex lh2 of purple bacterium rhodopseudomonas acidophila by monitoring sequences of fluorescence spectra of single lh2 assemblies, at room temperature, with different excitation intensities as well as at elevated temperatures, utilizing a confocal microscope. the fluorescence peak wavelength of individual lh2 complexes was found to abruptly move between long-lived quasi-stable levels differin ... | 2005 | 15501944 |
the "intracellular" poly(3-hydroxybutyrate) (phb) depolymerase of rhodospirillum rubrum is a periplasm-located protein with specificity for native phb and with structural similarity to extracellular phb depolymerases. | rhodospirillum rubrum possesses a putative intracellular poly(3-hydroxybutyrate) (phb) depolymerase system consisting of a soluble phb depolymerase, a heat-stable activator, and a 3-hydroxybutyrate dimer hydrolase (j. m. merrick and m. doudoroff, j. bacteriol. 88:60-71, 1964). in this study we reinvestigated the soluble r. rubrum phb depolymerase (phaz1). it turned out that phaz1 is a novel type of phb depolymerase with unique properties. purified phaz1 was specific for amorphous short-chain-len ... | 2004 | 15489436 |
expansion and compression of a protein folding intermediate by groel. | the groel-groes chaperonin system is required for the assisted folding of many essential proteins. the precise nature of this assistance remains unclear, however. here we show that denatured rubisco from rhodospirillum rubrum populates a stable, nonaggregating, and kinetically trapped monomeric state at low temperature. productive folding of this nonnative intermediate is fully dependent on groel, groes, and atp. reactivation of the trapped rubisco monomer proceeds through a series of groel-indu ... | 2004 | 15469819 |
variable lh2 stoichiometry and core clustering in native membranes of rhodospirillum photometricum. | the individual components of the photosynthetic unit (psu), the light-harvesting complexes (lh2 and lh1) and the reaction center (rc), are structurally and functionally known in great detail. an important current challenge is the study of their assembly within native membranes. here, we present afm topographs at 12 a resolution of native membranes containing all constituents of the psu from rhodospirillum photometricum. besides the major technical advance represented by the acquisition of such h ... | 2004 | 15457213 |
on the role of the carotenoids in photosynthesis in rhodospirillum rubrum. | 1950 | 15433994 | |
functional expression and characterization of a bacterial light-harvesting membrane protein in escherichia coli and cell-free synthesis systems. | heterologous expression of a bacterial light-harvesting (lh) integral membrane protein was attempted using escherichia coli cells and cell-free synthesis systems prepared from e. coli extracts. the alpha-apoprotein of lh1 complex from purple photosynthetic bacterium rhodospirillum rubrum was overexpressed as a recombinant protein with a histidine (his6) tag added to the carboxyl terminus. both of the expression systems produced alpha-apoprotein in a fully functional form as can judged by its abi ... | 2004 | 15388971 |
observation of calcium-dependent unidirectional rotational motion in recombinant photosynthetic f1-atpase molecules. | atp hydrolysis and synthesis by the f(0)f(1)-atp synthase are coupled to proton translocation across the membrane in the presence of magnesium. calcium is known, however, to disrupt this coupling in the photosynthetic enzyme in a unique way: it does not support atp synthesis, and caatp hydrolysis is decoupled from any proton translocation, but the membrane does not become leaky to protons. understanding the molecular basis of these calcium-dependent effects can shed light on the as yet unclear m ... | 2004 | 15377671 |
importance of rhodospirillum rubrum h(+)-pyrophosphatase under low-energy conditions. | the physiological role of the membrane-bound pyrophosphatase of rhodospirillum rubrum was investigated by the characterization of a mutant strain. comparisons of growth levels between the wild type and the mutant under different low-potential conditions and during transitions between different metabolisms indicate that this enzyme provides r. rubrum with an alternative energy source that is important for growth in low-energy states. | 2004 | 15375148 |
similarities between the abiotic reduction of selenite with glutathione and the dissimilatory reaction mediated by rhodospirillum rubrum and escherichia coli. | various mechanisms have been proposed to explain the biological dissimilatory reduction of selenite (seo3(2-)) to elemental selenium (se(o)), although none is without controversy. glutathione, the most abundant thiol in the eukaryotic cells, the cyanobacteria, and the alpha, beta, and gamma groups of the proteobacteria, has long been suspected to be involved in selenium metabolism. experiments with the phototrophic alpha proteobacterium rhodospirillum rubrum showed that the rate of selenite redu ... | 2004 | 15371444 |
the h(+)-pyrophosphatase of rhodospirillum rubrum is predominantly located in polyphosphate-rich acidocalcisomes. | acidocalcisomes are acidic, calcium storage compartments with a h(+) pump located in their membrane that have been described in several unicellular eukaryotes, including trypanosomatid and apicomplexan parasites, algae, and slime molds, and have also been found in the bacterium agrobacterium tumefaciens. in this work, we report that the h(+)-pyrophosphatase (h(+)-ppase) of rhodospirillum rubrum, the first enzyme of this type that was identified and thought to be localized only to chromatophore m ... | 2004 | 15371423 |
co-sensing mechanisms. | carbon monoxide (co) has long been known to have dramatic physiological effects on organisms ranging from bacteria to humans, but recently there have a number of suggestions that organisms might have specific sensors for co. this article reviews the current evidence for a variety of proteins with demonstrated or potential co-sensing ability. particular emphasis is placed on the molecular description of cooa, a heme-containing co sensor from rhodospirillum rubrum, since its biological role as a c ... | 2004 | 15353565 |
changing the ligand specificity of cooa, a highly specific heme-based co sensor. | the co-specific heme-based sensor cooa regulates the ability of rhodospirillum rubrum to grow on co as an energy source. only co triggers the conformational change of cooa essential for the protein to function as a transcriptional activator. a structurally informed mutagenesis, followed by an in vivo screening method, allowed the isolation of a series of novel cooa variants that show very substantial response to imidazole. compared with wild-type cooa, the ligand selectivity between imidazole an ... | 2004 | 15326187 |
the c-helix in cooa rolls upon co binding to ferrous heme. | cooa is a homodimeric transcriptional activator from rhodospirillum rubrum containing one heme in each subunit. co binding to the heme in its sensor domain activates cooa, facilitating the binding to dna by its dna-binding domain. the c-helix links the two domains and shapes an interface between the subunits. to probe the nature of co activation, residues at positions 112-121 on the c-helix were replaced by asn or gln and their effects were evaluated by resonance raman spectroscopy and by the me ... | 2004 | 15326178 |
circular dichroism of carotenoids in bacterial light-harvesting complexes: experiments and modeling. | in this work we investigate the origin and characteristics of the circular dichroism (cd) spectrum of rhodopin glucoside and lycopene in the light-harvesting 2 complex of rhodopseudomonas acidophila and rhodospirillum molischianum, respectively. we successfully model their absorption and cd spectra based on the high-resolution structures. we assume that these spectra originate from seven interacting transition dipole moments: the first corresponds to the 0-0 transition of the carotenoid, whereas ... | 2004 | 15326029 |
active-site conformational changes associated with hydride transfer in proton-translocating transhydrogenase. | transhydrogenase couples the redox (hydride-transfer) reaction between nad(h) and nadp(h) to proton translocation across a membrane. the redox reaction is catalyzed at the interface between two components (di and diii) which protrude from the membrane. a complex formed from recombinant di and diii (the di(2)diii(1) complex) from rhodospirillum rubrum transhydrogenase catalyzes fast single-turnover hydride transfer between bound nucleotides. in this report we describe three new crystal structures ... | 2004 | 15323555 |
hypercyst mutants in rhodospirillum centenum identify regulatory loci involved in cyst cell differentiation. | rhodospirillum centenum is a purple photosynthetic bacterium that forms resting cyst cells when starved for nutrients. in this study, we demonstrate that chalcone synthase gene (chsa) expression is developmentally regulated, with expression of chsa increasing up to 86-fold upon induction of the cyst developmental cycle. screening for mini-tn5-induced mutants that exhibit elevated chsa::lacz expression has led to the isolation of a set of r. centenum mutants that display increased chsa gene expre ... | 2004 | 15317789 |
the reaction center h subunit is not required for high levels of light-harvesting complex 1 in rhodospirillum rubrum mutants. | the gene (puha) encoding the h subunit of the reaction center (rc) was deleted by site-directed interposon mutagenesis by using a kanamycin resistance cassette lacking transcriptional terminators to eliminate polar effects in both the wild-type strain rhodospirillum rubrum s1 and the carotenoid-less strain r. rubrum g9. the puha interposon mutants were incapable of photoheterotrophic growth but grew normally under aerobic chemoheterotrophic conditions. absorption spectroscopy and sodium dodecyl ... | 2004 | 15317762 |
[an oligonucleotide primer system for amplification of the ribulose-1,5-bisphosphate carboxylase/oxygenase genes of bacteria of various taxonomic groups]. | based on the analysis of genbank nucleotide sequences of the cbbl and cbbm genes, coding for the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubpc), the key enzyme of the calvin cycle, a primer system was designed that allows about 800-bp-long fragments of these genes to be pcr-ampliflied in various photo- and chemotrophic bacteria. the efficiency of the designed primer system in detection of rubpc genes was demonstrated in pcr with dna of taxonomically diverse bacteria pos ... | 2004 | 15315232 |
use of iron anomalous scattering with multiple models and data sets to identify and refine a weak molecular replacement solution: structure analysis of cytochrome c' from two bacterial species. | the structure of cytochrome c' from two bacterial species, alcaligenes sp and alcaligenes denitrificans, have been determined from x-ray diffraction data to 3.0 a resolution using the anomalous scattering of the single fe atom in each to identify and refine a weak molecular-replacement solution. molecular-replacement studies, with the program amore, used two isomorphous data sets (from the two species), two independent search models (the cytochromes c' from rhodospirillum molischianum and rhodos ... | 1995 | 15299294 |
differential regulation of soluble and membrane-bound inorganic pyrophosphatases in the photosynthetic bacterium rhodospirillum rubrum provides insights into pyrophosphate-based stress bioenergetics. | soluble and membrane-bound inorganic pyrophosphatases (sppase and h(+)-ppase, respectively) of the purple nonsulfur bacterium rhodospirillum rubrum are differentially regulated by environmental growth conditions. both proteins and their transcripts were found in cells of anaerobic phototrophic batch cultures along all growth phases, although they displayed different time patterns. however, in aerobic cells that grow in the dark, which exhibited the highest growth rates, northern and western blot ... | 2004 | 15292143 |
activation mechanisms of transcriptional regulator cooa revealed by small-angle x-ray scattering. | cooa, a heme-containing transcriptional activator, binds co to the heme moiety and then undergoes a structural change that promotes the specific binding to the target dna. to elucidate the activation mechanism coupled to co binding, we investigated the co-dependent structural transition of cooa with small-angle x-ray scattering (saxs). in the absence of co, the radius of gyration rg and the second virial coefficient (a2) were 25.3(+/-0.5)a and -0.39(+/-0.25) x 10(-4)ml mol g(-2), respectively. c ... | 2004 | 15288777 |
oxygen-dependent h2o2 production by rubisco. | oxygen and ribulose-1,5-bisphosphate dependent, h(2)o(2) production was observed with several wild type rubisco enzymes using a sensitive assay. h(2)o(2) and d-glycero-2,3-pentodiulose-1,5-bisphosphate, a known and potent inhibitor of rubisco activity, are predicted products arising from elimination of h(2)o(2) from a peroxyketone intermediate, specific to oxygenase activity. parallel assays using varying co(2) and o(2) concentrations revealed that the partitioning to h(2)o(2) during o(2) consum ... | 2004 | 15280029 |
watching the photosynthetic apparatus in native membranes. | over the last 9 years, the structures of the various components of the bacterial photosynthetic apparatus or their homologues have been determined by x-ray crystallography to at least 4.8-a resolution. despite this wealth of structural information on the individual proteins, there remains an urgent need to examine the architecture of the photosynthetic apparatus in intact photosynthetic membranes. information on the arrangement of the different complexes in a native system will help us to unders ... | 2004 | 15273291 |
effect of sodium sulfide on ni-containing carbon monoxide dehydrogenases. | the structure of the active-site c-cluster in co dehydrogenase from carboxydothermus hydrogenoformans includes a mu(2)-sulfide ion bridged to the ni and unique fe, whereas the same cluster in enzymes from rhodospirillum rubrum (codh(rr)) and moorella thermoacetica (codh(mt)) lack this ion. this difference was investigated by exploring the effects of sodium sulfide on activity and spectral properties. sulfide partially inhibited the co oxidation activity of codh(rr) and generated a lag prior to s ... | 2004 | 15264843 |
the nitrogen-fixing gene (nifh) of rhodopseudomonas palustris: a case of lateral gene transfer? | nitrogen fixation is catalysed by some photosynthetic bacteria. this paper presents a phylogenetic comparison of a nitrogen fixation gene (nifh) with the aim of elucidating the processes underlying the evolutionary history of rhodopseudomonas palustris. in the nifh phylogeny, strains of rps. palustris were placed in close association with rhodobacter spp. and other phototrophic purple non-sulfur bacteria belonging to the alpha-proteobacteria, separated from its close relatives bradyrhizobium jap ... | 2004 | 15256566 |
the structure and function of bacterial light-harvesting complexes. | the harvesting of solar radiation by purple photosynthetic bacteria is achieved by circular, integral membrane pigment-protein complexes. there are two main types of light-harvesting complex, termed lh2 and lh1, that function to absorb light energy and to transfer that energy rapidly and efficiently to the photochemical reaction centres where it is trapped. this mini-review describes our present understanding of the structure and function of the purple bacterial light-harvesting complexes. | 2004 | 15204626 |
inhibition studies on rhodospirillum rubrum h(+)-pyrophosphatase expressed in escherichia coli. | the membrane-bound proton-pumping inorganic pyrophosphatase from rhodospirillum rubrum was heterologously expressed in escherichia coli c43(de3) cells and was inhibited by 4-bromophenacyl bromide (bpb), n,n'-dicyclohexylcarbodiimid (dccd), diethyl pyrocarbonate (depc) and fluorescein 5'-isothiocyanate (fitc). in each case, the enzyme activity was rather well protected against inhibitory action by the substrate mg(2)ppi. site-directed mutagenesis was employed in attempts to identify target residu ... | 2004 | 15178477 |
dual flagellar systems enable motility under different circumstances. | flagella are extremely effective organelles of locomotion used by a variety of bacteria and archaea. some bacteria, including aeromonas, azospirillum, rhodospirillum, and vibrio species, possess dual flagellar systems that are suited for movement under different circumstances. swimming in liquid is promoted by a single polar flagellum. swarming over surfaces or in viscous environments is enabled by the production of numerous peritrichous, or lateral, flagella. the polar flagellum is produced con ... | 2004 | 15170400 |
interactions stabilizing the structure of the core light-harvesting complex (lh1) of photosynthetic bacteria and its subunit (b820). | reconstitution experiments with a chemically synthesized core light-harvesting (lh1) beta-polypeptide analogue having 3-methylhistidine instead of histidine in the position that normally donates the coordinating ligand to bacteriochlorophyll (bchl) have provided the experimental data needed to assign to b820 one of the two possible alphabeta.2bchl pairs that are observed in the crystal structure of lh2 from phaeospirillum (formerly rhodospirillum) molischianum, the one with rings iii and v of bc ... | 2004 | 15170338 |
a genome phylogeny for mitochondria among alpha-proteobacteria and a predominantly eubacterial ancestry of yeast nuclear genes. | analyses of 55 individual and 31 concatenated protein data sets encoded in reclinomonas americana and marchantia polymorpha mitochondrial genomes revealed that current methods for constructing phylogenetic trees are insufficiently sensitive (or artifact-insensitive) to ascertain the sister of mitochondria among the current sample of eight alpha-proteobacterial genomes using mitochondrially-encoded proteins. however, rhodospirillum rubrum came as close to mitochondria as any alpha-proteobacterium ... | 2004 | 15155797 |
initial structure modification of tetrahedral to planar nickel(ii) in a nickel-iron-sulfur cluster related to the c-cluster of carbon monoxide dehydrogenase. | a method has been devised that creates a planar ni(ii) site from a tetrahedral site in a nife(3)s(4) cubane-type cluster. reaction of [(ph(3)p)nife(3)s(4)(ls(3))](2)(-) (2) with 1,2-bis(dimethylphosphino)ethane affords [(dmpe)nife(3)s(4)(ls(3))](2)(-) (3), isolated in ca. 45% yield as (et(4)n)(2)[3a].2.5mecn and (et(4)n)(2)[3b].0.25mecn, both of which occur in triclinic space group p. each crystalline form contains two crystallographically inequivalent clusters with the same overall structure bu ... | 2004 | 15149242 |
carbon monoxide induced decomposition of the active site [ni-4fe-5s] cluster of co dehydrogenase. | during the past two years, crystal structures of cu- and mo-containing carbon monoxide dehydrogenases (codhs) and ni- and fe-containing codhs have been reported. the active site of codhs from anaerobic bacteria (cluster c) is composed of ni, fe, and s for which crystallographic studies of the enzymes from carboxydothermus hydrogenoformans, rhodospirillum rubrum, and moorella thermoaceticarevealed structural similarities in the overall protein fold but showed substantial differences in the essent ... | 2004 | 15113209 |
elucidating the role of conserved glutamates in h+-pyrophosphatase of rhodospirillum rubrum. | h(+)-pyrophosphatase (h(+)-ppase) catalyzes pyrophosphate-driven proton transport against the electrochemical potential gradient in various biological membranes. all 50 of the known h(+)-ppase amino acid sequences contain four invariant glutamate residues. in this study, we use site-directed mutagenesis in conjunction with functional studies to determine the roles of the glutamate residues glu(197), glu(202), glu(550), and glu(649) in the h(+)-ppase of rhodospirillum rubrum (r-ppase). all residu ... | 2004 | 15107429 |
low-lying excited states of light-harvesting system ii in purple bacteria. | the low-lying excited states of a b850 ring of rhodospirillum (rs.) molischianum are determined accurately by a semiempirical indo/s method. results obtained are found to fit extremely well with a frenkel exciton model with long-range dipolar interactions, and the spatial size of the electron-hole pair is confirmed to fall predominantly within one bacteriochlorophyll with a small leakage to its nearest neighbors. more importantly, the nearest neighbor exciton coupling constants are found to be c ... | 2004 | 15089341 |
unraveling the function of the rhodospirillum rubrum activator of polyhydroxybutyrate (phb) degradation: the activator is a phb-granule-bound protein (phasin). | efficient hydrolysis of native poly(3-hydroxybutyrate) (nphb) granules in vitro by soluble phb depolymerase of rhodospirillum rubrum requires pretreatment of nphb with an activator compound present in r. rubrum cells (j. m. merrick and m. doudoroff, j. bacteriol. 88:60-71, 1964). edman sequencing of the purified activator (17.4 kda; matrix-assisted laser desorption ionization-time of flight mass spectrometry) revealed identity to a hypothetical protein deduced from a partially sequenced r. rubru ... | 2004 | 15060050 |
the fixabcx genes in rhodospirillum rubrum encode a putative membrane complex participating in electron transfer to nitrogenase. | in our efforts to identify the components participating in electron transport to nitrogenase in rhodospirillum rubrum, we used mini-tn5 mutagenesis followed by metronidazole selection. one of the mutants isolated, snt-1, exhibited a decreased growth rate and about 25% of the in vivo nitrogenase activity compared to the wild-type values. the in vitro nitrogenase activity was essentially wild type, indicating that the mutation affects electron transport to nitrogenase. sequencing showed that the t ... | 2004 | 15028689 |
roles of heme axial ligands in the regulation of co binding to cooa. | cooa is a co-dependent transcription factor of the bacterium rhodospirillum rubrum that contains a six-coordinate heme. it has as its heme axial ligands pro(2) and cys(75) in the ferric state and pro(2) and his(77) in the ferrous state. to probe the regulation of co binding and the ligand switching mechanism in cooa, we have prepared site-directed mutants in which the residues contributing the axial ligands are substituted. the properties of these mutants were investigated by resonance raman and ... | 2004 | 15026411 |
flexibility and size heterogeneity of the lh1 light harvesting complex revealed by atomic force microscopy: functional significance for bacterial photosynthesis. | previous electron microscopic studies of bacterial rclh1 complexes demonstrated both circular and elliptical conformations of the lh1 ring, and this implied flexibility has been suggested to allow passage of quinol from the q(b) site of the rc to the quinone pool prior to reduction of the cytochrome bc(1) complex. we have used atomic force microscopy to demonstrate that these are just two of many conformations for the lh1 ring, which displays large molecule-to-molecule variations, in terms of bo ... | 2004 | 14993213 |
dynamics of carbon monoxide binding to cooa. | cooa is a dimeric co-sensing heme protein from rhodospirillum rubrum. the heme iron in reduced cooa is six-coordinate; the axial ligands are his-77 and pro-2. co displaces pro-2 and induces a conformation change that allows cooa to bind dna and activate transcription of coo genes. equilibrium co binding is cooperative, with a hill coefficient of n = 1.4, p(50) = 2.2 microm, and estimated adair constants k(1) = 0.16 and k(2) = 1.3 microm(-1). the rates of co binding and release are both strongly ... | 2004 | 14990568 |
functionally critical elements of cooa-related co sensors. | cooa is a heme-containing transcriptional activator that enables rhodospirillum rubrum to sense and grow on co as a sole energy source. we have identified a number of cooa homologs through database searches, expressed these heterologously in escherichia coli, and monitored their ability to respond to co in vivo. further in vitro analysis of two cooa homologs from azotobacter vinelandii and carboxydothermus hydrogenoformans corroborated the in vivo data by revealing the ability of co to bind to t ... | 2004 | 14973040 |
identification of critical residues in glnb for its activation of nifa activity in the photosynthetic bacterium rhodospirillum rubrum. | the p(ii) regulatory protein family is unusually widely distributed, being found in all three domains of life. three p(ii) homologs called glnb, glnk, and glnj have been identified in the photosynthetic bacterium rhodospirillum rubrum. these have roles in at least four distinct functions, one of which is activation of the nitrogen fixation-specific regulatory protein nifa. the activation of nifa requires only the covalently modified (uridylylated) form of glnb. glnk and glnj are not involved. ho ... | 2004 | 14970346 |
characterization of altered regulation variants of dinitrogenase reductase-activating glycohydrolase from rhodospirillum rubrum. | in rhodospirillum rubrum, nitrogenase activity is subject to posttranslational regulation through the adenosine diphosphate (adp)-ribosylation of dinitrogenase reductase by dinitrogenase reductase adp-ribosyltransferase (drat) and dinitrogenase reductase-activating glycohydrolase (drag). to study the posttranslational regulation of drag, its gene was mutagenized and colonies screened for altered drag regulation. three different mutants were found and the drag variants displayed different biochem ... | 2004 | 14960312 |
studies on the metabolism of photosynthetic bacteria. xiv. quantitative relations between malate dissimilation, photoproduction of hydrogen, and nitrogen metabolism in rhodospirillum rubrum. | 1952 | 14934264 | |
properties of cell-free hydrogenases of escherichia coli and rhodospirillum rubrum. | 1952 | 14927554 | |
studies on the metabolism of photosynthetic bacteria. xii. comparative light and dark metabolism of acetate and carbonate by rhodospirillum rubrum. | 1952 | 14924662 | |
chromatophores of rhodospirillum rubrum. | 1952 | 14910754 | |
a comparative study of the light and dark fermentations of organic acids by rhodo-spirillum rubrum. | 1951 | 14824109 | |
nonequivalence of methyl and carboxyl groups in photometabolism of acetate by rhodospirillum rubrum. | 1951 | 14817280 |